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Literature summary for 1.3.1.12 extracted from

  • Shabalin, I.G.; Gritsunov, A.; Hou, J.; S?awek, J.; Miks, C.D.; Cooper, D.R.; Minor, W.; Christendat, D.
    Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain (2020), FEBS J., 287, 2235-2255 .
    View publication on PubMed
Search for more literature for 1.3.1.12

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of a ternary complex with NAD+ and tyrosine to 2.2 A resolution, a binary complex with tyrosine, and a structure of an isolated ACT domain dimer Bacillus anthracis

Inhibitors

Inhibitors Comment Organism Structure
L-tyrosine tyrosine binding to ACT domains inactivates the enzyme by blocking both substrate-binding sites and one NAD+ site with the ACT domain of one subunit. Interaction occurs with residues S333 and D315 for both ACT domains Bacillus anthracis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.045
-
 prephenate presence of 0.002 mM L-tyrosine, pH 7.5, 25°C Bacillus anthracis
0.056
-
 prephenate presence of 0.006 mM L-tyrosine, pH 7.5, 25°C Bacillus anthracis
0.057
-
 prephenate pH 7.5, 25°C Bacillus anthracis
0.237
-
 NAD+ pH 7.5, 25°C Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis Q81P63
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate + NAD+
-
 Bacillus anthracis 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
tyrA
-
 Bacillus anthracis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 presence of NAD+, NADH, NADP+, and NADPH does not significantly change the melting temperature Bacillus anthracis
41
-
 melting temperature Bacillus anthracis
51
-
 melting temperature, presence of 10 mM L-tyrosine Bacillus anthracis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5
-
 prephenate presence of 0.006mM L-tyrosine, pH 7.5, 25°C Bacillus anthracis
12.3
-
 prephenate presence of 0.002 mM L-tyrosine, pH 7.5, 25°C Bacillus anthracis
49
-
 prephenate pH 7.5, 25°C Bacillus anthracis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0015
-
 L-tyrosine pH 7.5, 25°C Bacillus anthracis

General Information

General Information Comment Organism
physiological function PDH is allosterically regulated by tyrosine binding to the ACT domains, resulting in an asymmetric conformation of the DPH dimer that sterically prevents prephenate binding to either active site Bacillus anthracis